5.B.11.  The One Electron Transmembrane Transfer Complex (TmcABCD) Family  

Pereira et al. 2006 reported that three membrane-bound redox complexes are present in Desulfovibrio spp., whose genes are not found in the genomes of other sulfate reducers such as Desulfotalea psycrophila and Archaeoglobus fulgidus. These complexes contain a periplasmic cytochrome c subunit of the cytochrome c3 family, and their presence in these organisms correlates with the presence of a pool of periplasmic cytochromes c3, also absent in the two other sulfate reducers mentioned above.  Pereira et al. 2006 isolated and characterized the first of such complexes, Tmc from D. vulgaris Hildenborough, which is associated with the tetraheme type II cytochrome c3. The isolated Tmc complex contains four dissimilar subunits, including the small TpIIc3 (TmcA), an integral membrane cytochrome b (TmcC), and two cytoplasmic proteins, an iron-sulfur protein (TmcB) and a tryptophan-rich protein (TmcD). Spectroscopic studies indicated the presence of eight hemes c and two hemes b in the complex, pointing to an A2BCD composition (TmcA2BCD). EPR analysis reveals the presence of a [4Fe4S]3+ center and up to three other iron-sulfur centers in the cytoplasmic subunits. Nearly full reduction of the redox centers in the Tmc complex could be obtained upon incubation with hydrogenase/TpIc(3), supporting the role of this complex in transmembrane transfer of electrons to sulfate in the cytoplasm, resulting from periplasmic oxidation of hydrogen concomitant with the reduction of sulfate (Pereira et al. 2006).

This family belongs to the Iron-Sulfur Protein (ISP) Superfamily.



Dörries, M., L. Wöhlbrand, M. Kube, R. Reinhardt, and R. Rabus. (2016). Genome and catabolic subproteomes of the marine, nutritionally versatile, sulfate-reducing bacterium Desulfococcus multivorans DSM 2059. BMC Genomics 17: 918.

Martins, M., C. Mourato, F.O. Morais-Silva, C. Rodrigues-Pousada, G. Voordouw, J.D. Wall, and I.A. Pereira. (2016). Electron transfer pathways of formate-driven H2 production in Desulfovibrio. Appl. Microbiol. Biotechnol. 100: 8135-8146.

Pereira, P.M., M. Teixeira, A.V. Xavier, R.O. Louro, and I.A. Pereira. (2006). The Tmc complex from Desulfovibrio vulgaris hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation. Biochemistry 45: 10359-10367.


TC#NameOrganismal TypeExample

Pentameric transmembrane electron flow carrier complex, TmcA2BCD.  TmcA is an acidic periplasmic cytochrome c3 of 126 aas and 0 TMSs anchored  to TmcC, TmcB is a ferridoxin/4Fe4S complex protein of 439 aas and 0 TMSs on the cytoplasmic side of the membrane, TmcC is a transmembrane protein of 219 aas and 5 TMSs, and TmcD is a cytochrome protein of 408 aas and 0 TMSs anchored to TmcC on the cytoplasmic side of the membrane.  This complex trasfers electrons resulting from the periplasmic oxidation of H2 to the cytoplasmic reduction of sulfate (Pereira et al. 2006). TmcA shows weak similarity to a constituent of 5.B.3.1.1, TmcB shows similarity to a constituent of 3.D.7.1.1 and TmcC shows weak similarity to a constituent of 5.A.3.1.2, but TmcD does not show similarity to consitutents of other systems in TCDB.

TmcABCD of Desulfovibrio vulgaris


The three component TmcA1B1C1 electron transfer complex from sulfate-reducing bacteria, TmcA1,B1,C1 (Dörries et al. 2016). Transfers electrons from the periplasm to the cytoplasm for sulfate reduction.

TmcA1B1C1 of Desulfococcus multivorans
TmcA1, 132 aas with 1 N-terminal TMS, AOY57579, an acidic cytochrome c.
TmcB1, 445 aas and 0 TMSs, AOY57578, a cytoplasmic iron-sulfur protein
TmcC1, 219 aas and 5 TMSs, AOY57577, an uncharacterized protein of the Tmc complex